Structure of Proteins Flashcards

1
Q

chains of amino acids

A

proteins

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2
Q

what makes amino acids different from each other in both structure and function?

A

different functional groups

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3
Q

how many major classes of proteins are there? Enumerate.

A
6
Catalyst
Transport and Storage
Structural
Movement
Regulation of Metabolism and Gene Expression
Protection
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4
Q

How do catalysts work?

A

accelerates the rate of reaction by lowering the activation energy without being part of the actual reaction

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5
Q

Contain 2-10 AA

A

Peptides

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6
Q

Contain 10-100 AA

A

Polypeptides

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7
Q

Contain more than 100 AAs

A

Proteins

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8
Q

The biologically relevant enantiomer

A

Levorotatory AAs

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9
Q

Why are AAs dependent on their R groups?

A

R groups dictate chemical reactivity and electric charge

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10
Q

What is an AA composed of?

A

Amino group
Carboxyl group
Side chain

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11
Q

What causes sickle cell anemia?

A

Substitution of polar glutamate by nonpolar valine at the sixth position in the B unit of hemoglobin

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12
Q

Zwitter ion?

A

when the ion itself is charged but the net charge is zero

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13
Q

When the pH is greater than pI then the AAs net charge is _________.

A

negative

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14
Q

Useful when we’re looking for the pH where the zwitter ion will be formed
Equal to the pH when net charge is 0

A

Isoelectric point

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15
Q

Bonds that link AAs to form peptides

A

Amide Bonds

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16
Q

Peptide formation is a ________ reaction. Therefore to break the bonds you would need _______.

A

condensation

hydrolysis

17
Q

Can come in to aid in proper protein folding

A

chaperones

chaperonins

18
Q

Describe the alpha helix structure dude.

A

3.6 residues
polar on one side
non polar on the other
side chains go out

19
Q

how are B sheets formed

A

they’re linked by H bonds

20
Q

cause the reversal of direction of their polypeptide chains
also causes globular shape
also also connects helices and sheets

A

Bturns

21
Q

exemption from a helix formation because steric

A

WTF IVY

22
Q

exemption from a helix formation because H bond

A

NDPSG

23
Q

proteins that are insoluble and usually take structural roles

A

fibrous protein

24
Q

water soluble proteins with biological roles

A

globular proteins

25
Q

undergoes extensive modification and post translational modification from the er to the cytosol and to the extracellular space. Not keratin

A

Collagen

26
Q

a compound with a functional group that contains a carbon-nitrogen double bond with the nitrogen atom connected to an aryl or alkyl group, not hydrogen

A

schiff base